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[PMID]:29338047
[Au] Autor:Hsia HP; Yang YH; Szeto WC; Nilsson BE; Lo CY; Ng AK; Fodor E; Shaw PC
[Ad] Endereço:Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China.
[Ti] Título:Amino acid substitutions affecting aspartic acid 605 and valine 606 decrease the interaction strength between the influenza virus RNA polymerase PB2 '627' domain and the viral nucleoprotein.
[So] Source:PLoS One;13(1):e0191226, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The influenza virus RNA genome is transcribed and replicated in the context of the viral ribonucleoprotein (vRNP) complex by the viral RNA polymerase. The nucleoprotein (NP) is the structural component of the vRNP providing a scaffold for the viral RNA. In the vRNP as well as during transcription and replication the viral polymerase interacts with NP but it is unclear which parts of the polymerase and NP mediate these interactions. Previously the C-terminal '627' domain (amino acids 538-693) of PB2 was shown to interact with NP. Here we report that a fragment encompassing amino acids 146-185 of NP is sufficient to mediate this interaction. Using NMR chemical shift perturbation assays we show that amino acid region 601 to 607 of the PB2 '627' domain interacts with this fragment of NP. Substitutions of these PB2 amino acids resulted in diminished RNP activity and surface plasmon resonance assays showed that amino acids D605 was essential for the interaction with NP and V606 may also play a partial role in the interaction. Collectively these results reveal a possible interaction surface between NP and the PB2 subunit of the RNA polymerase complex.
[Mh] Termos MeSH primário: Vírus da Influenza A Subtipo H5N1/química
Vírus da Influenza A Subtipo H5N1/genética
RNA Replicase/química
RNA Replicase/genética
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas do Core Viral/química
Proteínas do Core Viral/genética
Proteínas Virais/química
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Ácido Aspártico/química
Genoma Viral
Células HEK293
Seres Humanos
Vírus da Influenza A Subtipo H5N1/fisiologia
Influenza Humana/virologia
Modelos Moleculares
Ressonância Magnética Nuclear Biomolecular
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Ressonância de Plasmônio de Superfície
Valina/química
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NP protein, Influenza A virus); 0 (PB2 protein, Influenzavirus A); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 0 (Viral Core Proteins); 0 (Viral Proteins); 30KYC7MIAI (Aspartic Acid); EC 2.7.7.48 (RNA Replicase); HG18B9YRS7 (Valine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191226


  2 / 5552 MEDLINE  
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[PMID]:29042217
[Au] Autor:Pleshakova TO; Kaysheva AL; Bayzyanova JМ; Anashkina АS; Uchaikin VF; Ziborov VS; Konev VA; Archakov AI; Ivanov YD
[Ad] Endereço:Institute of Biomedical Chemistry, Pogodinskaya St. 10, Moscow, 119121, Russia.
[Ti] Título:The detection of hepatitis c virus core antigen using afm chips with immobolized aptamers.
[So] Source:J Virol Methods;251:99-105, 2018 Jan.
[Is] ISSN:1879-0984
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In the present study, the possibility of hepatitis C virus core antigen (HCVcoreAg) detection in buffer solution, using atomic force microscope chip (AFM-chip) with immobilized aptamers, has been demonstrated. The target protein was detected in 1mL of solution at concentrations from 10 М to 10 М. The registration of aptamer/antigen complexes on the chip surface was carried out by atomic force microscopy (AFM). The further mass-spectrometric (MS) identification of AFM-registered objects on the chip surface allowed reliable identification of HCVcoreAg target protein in the complexes. Aptamers, which were designed for therapeutic purposes, have been shown to be effective in HCVcoreAg detection as probe molecules.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/metabolismo
Microscopia de Força Atômica/métodos
Proteínas do Core Viral/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aptamers, Nucleotide); 0 (Viral Core Proteins); 0 (nucleocapsid protein, Hepatitis C virus)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE


  3 / 5552 MEDLINE  
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[PMID]:29040311
[Au] Autor:Kondoh T; Manzoor R; Nao N; Maruyama J; Furuyama W; Miyamoto H; Shigeno A; Kuroda M; Matsuno K; Fujikura D; Kajihara M; Yoshida R; Igarashi M; Takada A
[Ad] Endereço:Division of Global Epidemiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo, Japan.
[Ti] Título:Putative endogenous filovirus VP35-like protein potentially functions as an IFN antagonist but not a polymerase cofactor.
[So] Source:PLoS One;12(10):e0186450, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It has been proposed that some non-retroviral RNA virus genes are integrated into vertebrate genomes. Endogenous filovirus-like elements (EFLs) have been discovered in some mammalian genomes. However, their potential roles in ebolavirus infection are unclear. A filovirus VP35-like element (mlEFL35) is found in the little brown bat (Myotis lucifugus) genome. Putative mlEFL35-derived protein (mlEFL35p) contains nearly full-length amino acid sequences corresponding to ebolavirus VP35. Ebola virus VP35 has been shown to bind double-stranded RNA, leading to inhibition of type I interferon (IFN) production, and is also known as a viral polymerase cofactor that is essential for viral RNA transcription/replication. In this study, we transiently expressed mlEFL35p in human kidney cells and investigated its biological functions. We first found that mlEFL35p was coimmunoprecipitated with itself and ebolavirus VP35s but not with the viral nucleoprotein. Then the biological functions of mlEFL35p were analyzed by comparing it to ebolavirus VP35s. We found that the expression of mlEFL35p significantly inhibited human IFN-ß promoter activity as well as VP35s. By contrast, expression of mlEFL35p did not support viral RNA transcription/replication and indeed slightly decrease the reporter gene expression in a minigenome assay. These results suggest that mlEFL35p potentially acts as an IFN antagonist but not a polymerase cofactor.
[Mh] Termos MeSH primário: Ebolavirus/genética
Interações Hospedeiro-Patógeno
Interferon beta/antagonistas & inibidores
Nucleoproteínas/genética
RNA de Cadeia Dupla/genética
Proteínas do Core Viral/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Quirópteros/virologia
Ebolavirus/isolamento & purificação
Ebolavirus/metabolismo
Expressão Gênica
Genes Reporter
Células HEK293
Seres Humanos
Interferon beta/genética
Interferon beta/imunologia
Luciferases/genética
Luciferases/metabolismo
Nucleoproteínas/metabolismo
Regiões Promotoras Genéticas
Ligação Proteica
RNA de Cadeia Dupla/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Proteínas do Core Viral/metabolismo
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleoproteins); 0 (RNA, Double-Stranded); 0 (Recombinant Proteins); 0 (Viral Core Proteins); 0 (nucleoprotein VP35, Ebola virus); 77238-31-4 (Interferon-beta); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186450


  4 / 5552 MEDLINE  
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[PMID]:28917841
[Au] Autor:Gc JB; Pokhrel R; Bhattarai N; Johnson KA; Gerstman BS; Stahelin RV; Chapagain PP
[Ad] Endereço:Department of Physics, Florida International University, Miami, FL 33199, United States.
[Ti] Título:Graphene-VP40 interactions and potential disruption of the Ebola virus matrix filaments.
[So] Source:Biochem Biophys Res Commun;493(1):176-181, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ebola virus infections cause hemorrhagic fever that often results in very high fatality rates. In addition to exploring vaccines, development of drugs is also essential for treating the disease and preventing the spread of the infection. The Ebola virus matrix protein VP40 exists in various conformational and oligomeric forms and is a potential pharmacological target for disrupting the virus life-cycle. Here we explored graphene-VP40 interactions using molecular dynamics simulations and graphene pelleting assays. We found that graphene sheets associate strongly with VP40 at various interfaces. We also found that the graphene is able to disrupt the C-terminal domain (CTD-CTD) interface of VP40 hexamers. This VP40 hexamer-hexamer interface is crucial in forming the Ebola viral matrix and disruption of this interface may provide a method to use graphene or similar nanoparticle based solutions as a disinfectant that can significantly reduce the spread of the disease and prevent an Ebola epidemic.
[Mh] Termos MeSH primário: Grafite/química
Nucleoproteínas/química
Nucleoproteínas/ultraestrutura
Proteínas do Core Viral/química
Proteínas do Core Viral/ultraestrutura
Proteínas da Matriz Viral/química
Proteínas da Matriz Viral/ultraestrutura
[Mh] Termos MeSH secundário: Sítios de Ligação
Simulação de Dinâmica Molecular
Ligação Proteica
Conformação Proteica
Multimerização Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleoproteins); 0 (VP40 protein, virus); 0 (Viral Core Proteins); 0 (Viral Matrix Proteins); 0 (nucleoprotein VP40, Ebola virus); 7782-42-5 (Graphite)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170918
[St] Status:MEDLINE


  5 / 5552 MEDLINE  
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[PMID]:28915404
[Au] Autor:Lier C; Becker S; Biedenkopf N
[Ad] Endereço:Institute of Virology, Philipps-University Marburg, Marburg, Germany; German Center of Infection Research (DZIF), Partner Site Giessen-Marburg-Langen, Marburg, Germany.
[Ti] Título:Dynamic phosphorylation of Ebola virus VP30 in NP-induced inclusion bodies.
[So] Source:Virology;512:39-47, 2017 Dec.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Zaire Ebolavirus (EBOV) causes a severe feverish disease with high case fatality rates. Transcription of EBOV is dependent on the activity of the nucleocapsid protein VP30 which represents an essential viral transcription factor. Activity of VP30 is regulated via phosphorylation at six N-terminal serine residues. Recent data demonstrated that dynamic phosphorylation and dephosphorylation of serine residue 29 is essential for transcriptional support activity of VP30. To analyze the spatio/temporal dynamics of VP30 phosphorylation, we generated a peptide antibody recognizing specifically VP30 phosphorylated at serine 29. Using this antibody we could demonstrate that (i) the majority of VP30 molecules in EBOV-infected cells is dephosphorylated at the crucial position serine 29, (ii) both, VP30 phosphorylation and dephosphorylation take place in viral inclusion bodies that are induced by the nucleoprotein NP and (iii) NP influences the phosphorylation state of VP30.
[Mh] Termos MeSH primário: Corpos de Inclusão Viral/fisiologia
Nucleoproteínas/metabolismo
Fatores de Transcrição/metabolismo
Proteínas do Core Viral/metabolismo
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Regulação Viral da Expressão Gênica/fisiologia
Seres Humanos
Fosforilação
Fatores de Transcrição/genética
Proteínas Virais/genética
Replicação Viral/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleoproteins); 0 (Transcription Factors); 0 (VP30 protein, ebola virus); 0 (Viral Core Proteins); 0 (Viral Proteins); 0 (nucleoprotein VP35, Ebola virus)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE


  6 / 5552 MEDLINE  
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Villanova, Marcia Guimaräes
Martinelli, Ana de Lourdes Candolo
Texto completo SciELO Brasil
[PMID]:28902288
[Au] Autor:Chachá SGF; Gomes-Gouvêa MS; Malta FM; Ferreira SDC; Villanova MG; Souza FF; Teixeira AC; Passos ADDC; Pinho JRR; Martinelli ALC
[Ad] Endereço:Universidade Federal de São Carlos, Departamento de Medicina, São Carlos, SP, Brasil.
[Ti] Título:Basal core promoter and precore mutations among hepatitis B virus circulating in Brazil and its association with severe forms of hepatic diseases.
[So] Source:Mem Inst Oswaldo Cruz;112(9):626-631, 2017 Sep.
[Is] ISSN:1678-8060
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In Brazil, few studies have investigated the prevalence of infection with the precore (PC) and basal core promoter (BCP) mutants of the hepatitis B virus (HBV). OBJECTIVES: This study aimed to analyse the frequency of PC and BCP mutations among patients infected with HBV and to evaluate the association between the variants and advanced hepatic disease. METHODS: A total of 161 patients infected with HBV were studied. To identify PC and BCP mutations, a 501-bp fragment of HBV DNA was amplified and sequenced. FINDINGS: PC and BCP regions from HBV strains were successfully amplified and sequenced in 129 and 118 cases, respectively. PC and BCP mutations were detected in 61.0% and 80.6% of the cases, respectively. The A1762T/G1764A variant was identified in 36.7% of the patients with grade 1 and 2 liver fibrosis (29/79) and in 81.8% of the patients with grade 3 and 4 liver fibrosis (9/11) (p < 0.01); in 76.9% of the patients with cirrhosis (10/13) and in 38.1% of the patients without cirrhosis (40/105) (p = 0.01); and in 77.8% of the patients with hepatocellular carcinoma (HCC) (7/9) and in 39.4% of the patients without HCC (43/109) (p = 0.03). MAIN CONCLUSIONS: A high prevalence of HBV PC and BCP mutants was found. The A1762T/G1764A variant was independently associated with advanced forms of liver fibrosis, hepatic cirrhosis, and HCC.
[Mh] Termos MeSH primário: Vírus da Hepatite B/genética
Hepatite B Crônica/virologia
Cirrose Hepática/virologia
Mutação
Proteínas do Core Viral/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
DNA Viral
Feminino
Genótipo
Seres Humanos
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Viral Core Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE


  7 / 5552 MEDLINE  
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[PMID]:28880890
[Au] Autor:Eichwald C; Kim J; Nibert ML
[Ad] Endereço:Department of Microbiology & Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.
[Ti] Título:Dissection of mammalian orthoreovirus µ2 reveals a self-associative domain required for binding to microtubules but not to factory matrix protein µNS.
[So] Source:PLoS One;12(9):e0184356, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian orthoreovirus protein µ2 is a component of the viral core particle. Its activities include RNA binding and hydrolysis of the γ-phosphate from NTPs and RNA 5´-termini, suggesting roles as a cofactor for the viral RNA-dependent RNA polymerase, λ3, first enzyme in 5´-capping of viral plus-strand RNAs, and/or prohibitory of RNA-5´-triphosphate-activated antiviral signaling. Within infected cells, µ2 also contributes to viral factories, cytoplasmic structures in which genome replication and particle assembly occur. By associating with both microtubules (MTs) and viral factory matrix protein µNS, µ2 can anchor the factories to MTs, the full effects of which remain unknown. In this study, a protease-hypersensitive region allowed µ2 to be dissected into two large fragments corresponding to residues 1-282 and 283-736. Fusions with enhanced green fluorescent protein revealed that these amino- and carboxyl-terminal regions of µ2 associate in cells with either MTs or µNS, respectively. More exhaustive deletion analysis defined µ2 residues 1-325 as the minimal contiguous region that associates with MTs in the absence of the self-associating tag. A region involved in µ2 self-association was mapped to residues 283-325, and self-association involving this region was essential for MT-association as well. Likewise, we mapped that µNS-binding site in µ2 relates to residues 290-453 which is independent of µ2 self-association. These findings suggest that µ2 monomers or oligomers can bind to MTs and µNS, but that self-association involving µ2 residues 283-325 is specifically relevant for MT-association during viral factories formation.
[Mh] Termos MeSH primário: Microtúbulos/metabolismo
Orthoreovirus de Mamíferos/metabolismo
Proteínas não Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Cercopithecus aethiops
Citoplasma/metabolismo
Microscopia de Fluorescência
Ligação Proteica
RNA Viral/metabolismo
Proteínas do Core Viral/metabolismo
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Viral); 0 (Viral Core Proteins); 0 (Viral Nonstructural Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184356


  8 / 5552 MEDLINE  
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[PMID]:28820612
[Au] Autor:Moriishi K
[Ad] Endereço:a Department of Microbiology, Graduate School of Medical Science , University of Yamanashi , Yamanashi , Japan.
[Ti] Título:The potential of signal peptide peptidase as a therapeutic target for hepatitis C.
[So] Source:Expert Opin Ther Targets;21(9):827-836, 2017 Sep.
[Is] ISSN:1744-7631
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Chronic infection with hepatitis C virus (HCV) causes liver steatosis, cirrhosis, metabolic syndrome with inflammation, and eventually leads to hepatocellular carcinoma. HCV core protein is a well-known capsid protein and pathogenic factor related to lipid accumulation, type 2 diabetes mellitus, and carcinogenesis. Cleavage of the C-terminal transmembrane region by signal peptide peptidase (SPP) is required for maturation of the core protein. Areas covered: Herein, this review details the general aspects of the structure, lifecycle, pathogenesis, and maturation of the HCV core protein, the function of SPP, and clinically available direct-acting antivirals (DAAs). SPP is classified into a group of GXGD-type intramembrane proteases including presenilin-1, which is a component of γ-secretase complex. Several SPP inhibitors were previously identified from γ-secretase inhibitors, but have not yet been improved based on specificity to SPP. Finally, the author discusses the potential of SPP inhibitors for hepatitis C therapy. Expert opinion: Currently available DAAs therapies are limited because of different viral genotypes and underlying conditions in each patient. DAA-resistant viruses have also been reported. Development of SPP-selective inhibitors may improve current HCV therapies by decreasing in the emergence of DAA-resistant viruses irrespective of viral genotype.
[Mh] Termos MeSH primário: Antivirais/farmacologia
Ácido Aspártico Endopeptidases/metabolismo
Hepatite C Crônica/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Desenho de Drogas
Farmacorresistência Viral
Genótipo
Hepacivirus/genética
Hepatite C Crônica/enzimologia
Hepatite C Crônica/virologia
Seres Humanos
Terapia de Alvo Molecular
Proteínas do Core Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Viral Core Proteins); 0 (nucleocapsid protein, Hepatitis C virus); EC 3.4.23.- (Aspartic Acid Endopeptidases); EC 3.4.23.- (signal peptide peptidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170904
[Lr] Data última revisão:
170904
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170819
[St] Status:MEDLINE
[do] DOI:10.1080/14728222.2017.1369959


  9 / 5552 MEDLINE  
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[PMID]:28795465
[Au] Autor:Lee LS; Brunk N; Haywood DG; Keifer D; Pierson E; Kondylis P; Wang JC; Jacobson SC; Jarrold MF; Zlotnick A
[Ad] Endereço:Molecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana, 47405.
[Ti] Título:A molecular breadboard: Removal and replacement of subunits in a hepatitis B virus capsid.
[So] Source:Protein Sci;26(11):2170-2180, 2017 Nov.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatitis B virus (HBV) core protein is a model system for studying assembly and disassembly of icosahedral structures. Controlling disassembly will allow re-engineering the 120 subunit HBV capsid, making it a molecular breadboard. We examined removal of subunits from partially crosslinked capsids to form stable incomplete particles. To characterize incomplete capsids, we used two single molecule techniques, resistive-pulse sensing and charge detection mass spectrometry. We expected to find a binomial distribution of capsid fragments. Instead, we found a preponderance of 3 MDa complexes (90 subunits) and no fragments smaller than 3 MDa. We also found 90-mers in the disassembly of uncrosslinked HBV capsids. 90-mers seem to be a common pause point in disassembly reactions. Partly explaining this result, graph theory simulations have showed a threshold for capsid stability between 80 and 90 subunits. To test a molecular breadboard concept, we showed that missing subunits could be refilled resulting in chimeric, 120 subunit particles. This result may be a means of assembling unique capsids with functional decorations.
[Mh] Termos MeSH primário: Capsídeo/ultraestrutura
Vírus da Hepatite B/ultraestrutura
Subunidades Proteicas/química
Proteínas do Core Viral/química
[Mh] Termos MeSH secundário: Compostos de Boro/química
Capsídeo/química
Simulação por Computador
Etilmaleimida/química
Corantes Fluorescentes/química
Vírus da Hepatite B/química
Espectrometria de Massas/métodos
Peso Molecular
Método de Monte Carlo
Multimerização Proteica
Cloreto de Sódio/química
Eletricidade Estática
Ureia/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (4,4-difluoro-4-bora-3a,4a-diaza-s-indacene); 0 (Boron Compounds); 0 (Fluorescent Dyes); 0 (Protein Subunits); 0 (Viral Core Proteins); 451W47IQ8X (Sodium Chloride); 8W8T17847W (Urea); O3C74ACM9V (Ethylmaleimide)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3265


  10 / 5552 MEDLINE  
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[PMID]:28783500
[Au] Autor:Wu Q; Li Z; Liu Q
[Ad] Endereço:Vaccine and Infectious Disease Organization-International Vaccine Center (VIDO-InterVac), University of Saskatchewan, 120 Veterinary Road, Saskatoon, Saskatchewan, Canada S7N 5E3; Department of Veterinary Microbiology, University of Saskatchewan, Saskatoon, Saskatchewan, Canada.
[Ti] Título:Treatment with PTEN-Long protein inhibits hepatitis C virus replication.
[So] Source:Virology;511:1-8, 2017 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatitis C virus (HCV) infection is a confirmed risk factor for hepatocellular carcinoma (HCC). Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) possesses tumor suppression function that is frequently defective in HCC tumors. PTEN-Long, a translation isoform of PTEN, functions in a cell non-autonomous manner. In this study, we demonstrated that intracellular overexpression of PTEN-Long inhibits HCV replication. More importantly, we showed that treatment with extracellular PTEN-Long protein inhibits HCV replication in a dose-dependent manner. Furthermore, we showed that PTEN-Long interacts with HCV core protein and this interaction is required for HCV replication inhibition by PTEN-Long. In summary, we demonstrated, for the first time, that PTEN-Long protein, an isoform of the canonical PTEN and in the form of extracellular protein treatment, inhibits HCV replication. Our study offers an opportunity for developing additional anti-HCV agents.
[Mh] Termos MeSH primário: Expressão Gênica
Hepacivirus/fisiologia
PTEN Fosfo-Hidrolase/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Antivirais/farmacologia
Carcinoma Hepatocelular/virologia
Linhagem Celular Tumoral
Seres Humanos
Neoplasias Hepáticas/virologia
PTEN Fosfo-Hidrolase/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas do Core Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Recombinant Proteins); 0 (Viral Core Proteins); 0 (nucleocapsid protein, Hepatitis C virus); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE



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